Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Site-specific hydrogen exchange of proteins: insights into the structures of amyloidogenic intermediates.

Methods in enzymology - 1 Jan 2005

Yao Zhong-Ping, Tito Paula, Robinson Carol V

Abstract excerpt

We describe the use of nano-electrospray ionization (nano-ESI) mass spectrometry (MS) for monitoring hydrogen exchange. Using this approach, we have compared the fluctuations in structure of the wild-type human lysozyme with those of the Asp67His and Ile56Thr variants, the two amyloidogenic forms...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amyloid
Share to Deuterium Exchange Measurement
Share to Hydrogen

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muramidase

Share to Nanotechnology

Share to Protein Folding

Share to Spectrometry, Mass, Electrospray Ionization

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Identifiers

PMID: 16401516
DOI: 10.1016/S0076-6879(05)02012-4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16401516-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Site-specific hydrogen exchange of proteins: insights into the structures of amyloidogenic intermediates.PMID 16401516Read ↗

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme.Semantic proximity Read ↗

Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.Semantic proximity Read ↗

Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Semantic proximity Read ↗

The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme.Semantic proximity Read ↗

Systematic conformation-to-phenotype mapping via limited deep-sequencing of proteinsSemantic proximity Read ↗

Probing serpin conformational change using mass spectrometry and related methods.Semantic proximity Read ↗

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations.Semantic proximity Read ↗

Engineering a Camelid Antibody Fragment That Binds to the Active Site of Human Lysozyme and Inhibits Its Conversion into Amyloid FibrilsSemantic proximity Read ↗

Parsing disease-relevant protein modifications from epiphenomena: perspective on the structural basis of SOD1-mediated ALS.Semantic proximity Read ↗

Probing local structural fluctuations in myoglobin by size-dependent thiol-disulfide exchange.Semantic proximity Read ↗

Amyloid forming human lysozyme intermediates are stabilised by non-native amide-π interactionsSemantic proximity Read ↗

Mass spectrometry footprinting reveals how kinetic stabilizers counteract transthyretin dynamics altered by pathogenic mutations.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.